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Protein

Microsomal triglyceride transfer protein large subunit

Gene

MTTP

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the transport of triglyceride, cholesteryl ester, and phospholipid between phospholipid surfaces (PubMed:23475612, PubMed:8939939, PubMed:26224785, PubMed:25108285, PubMed:22236406). Required for the secretion of plasma lipoproteins that contain apolipoprotein B (PubMed:23475612, PubMed:8939939, PubMed:26224785).5 Publications

GO - Molecular functioni

  • lipid binding Source: UniProtKB-KW
  • lipid transporter activity Source: UniProtKB
  • phospholipid transporter activity Source: UniProtKB
  • protein heterodimerization activity Source: UniProtKB

GO - Biological processi

  • lipid metabolic process Source: ProtInc
  • lipoprotein biosynthetic process Source: Reactome
  • phospholipid transport Source: UniProtKB
  • plasma lipoprotein particle assembly Source: UniProtKB
  • triglyceride transport Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Transport

Keywords - Ligandi

Lipid-binding

Enzyme and pathway databases

BioCyciZFISH:ENSG00000138823-MONOMER.
ReactomeiR-HSA-174800. Chylomicron-mediated lipid transport.
R-HSA-8866423. VLDL biosynthesis.

Chemistry databases

SwissLipidsiSLP:000000411.

Names & Taxonomyi

Protein namesi
Recommended name:
Microsomal triglyceride transfer protein large subunit
Gene namesi
Name:MTTP
Synonyms:MTP
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 4

Organism-specific databases

HGNCiHGNC:7467. MTTP.

Subcellular locationi

GO - Cellular componenti

  • endoplasmic reticulum Source: UniProtKB
  • endoplasmic reticulum lumen Source: Reactome
  • receptor complex Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum

Pathology & Biotechi

Involvement in diseasei

Abetalipoproteinemia (ABL)7 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn autosomal recessive disorder of lipoprotein metabolism. Affected individuals produce virtually no circulating apolipoprotein B-containing lipoproteins (chylomicrons, VLDL, LDL, lipoprotein(A)). Malabsorption of the antioxidant vitamin E occurs, leading to spinocerebellar and retinal degeneration.
See also OMIM:200100
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_074553169D → V in ABL; no loss on localization to the endoplasmic reticulum; does not reduce interaction with APOB; inhibits interaction with P4HB/PDI; inhibits phospholipid or triglyceride transfer activity; inhibits apolipoprotein B secretion. 1 Publication1
Natural variantiVAR_074554264G → R in ABL; unknown pathological significance; does not reduce interaction with P4HB/PDI and APOB; does not reduce triglyceride transfer activity. 1 Publication1
Natural variantiVAR_074555435L → H in ABL; no loss on localization to the endoplasmic reticulum; inhibits triglyceride transfer activity. 1 Publication1
Natural variantiVAR_074556528Y → H in ABL; does not reduce interaction with P4HB/PDI and APOB; inhibits triglyceride transfer activity. 1 Publication1
Natural variantiVAR_074557540R → C in ABL; does not reduce interaction with P4HB/PDI and APOB; inhibits triglyceride transfer activity. 1 PublicationCorresponds to variant rs372321643dbSNPEnsembl.1
Natural variantiVAR_010642540R → H in ABL; no loss on localization to the endoplasmic reticulum; reduces interaction with P4HB/PDI; inhibits phospholipid or triglyceride transfer activity; inhibits apolipoprotein B secretion. 4 PublicationsCorresponds to variant rs199422220dbSNPEnsembl.1
Natural variantiVAR_010643590S → I in ABL; no loss on localization to the endoplasmic reticulum; does not reduce interaction with P4HB/PDI; inhibits phospholipid or triglyceride transfer activity; inhibits apolipoprotein B secretion. 2 PublicationsCorresponds to variant rs199422222dbSNPEnsembl.1
Natural variantiVAR_074558649N → S in ABL; unknown pathological significance; does not reduce interaction with P4HB/PDI and APOB; reduces triglyceride transfer activity. 1 Publication1
Natural variantiVAR_010644746G → E in ABL; no loss on localization to the endoplasmic reticulum; does not reduce interaction with P4HB/PDI; inhibits phospholipid or triglyceride transfer activity; inhibits apolipoprotein B secretion. 2 PublicationsCorresponds to variant rs767833468dbSNPEnsembl.1
Natural variantiVAR_014019780N → Y in ABL; no loss on localization to the endoplasmic reticulum; does not reduce interaction with P4HB/PDI; inhibits phospholipid or triglyceride transfer activity; inhibits apolipoprotein B secretion. 2 PublicationsCorresponds to variant rs199422221dbSNPEnsembl.1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi169D → E: No loss on localization to the endoplasmic reticulum and does not reduce interaction with APOB or P4HB/PDI, does partially reduce phospholipid or triglyceride transfer activity and apolipoprotein B secretion. 1 Publication1
Mutagenesisi187K → L: No loss on localization to the endoplasmic reticulum and does not reduce interaction with APOB, but inhibits interaction with P4HB/PDI, phospholipid or triglyceride transfer activity and apolipoprotein B secretion. 1 Publication1
Mutagenesisi187K → R: No loss on localization to the endoplasmic reticulum, does not reduce interaction with APOB or P4HB/PDI, partially inhibits triglyceride transfer activity, does not inhibit phospholipid transfer activity and apolipoprotein B secretion. 1 Publication1
Mutagenesisi189K → L: No loss on localization to the endoplasmic reticulum and does not reduce interaction with APOB, but inhibits interaction with P4HB/PDI, phospholipid or triglyceride transfer activity and apolipoprotein B secretion. 1 Publication1
Mutagenesisi189K → R: No loss on localization to the endoplasmic reticulum, does not reduce interaction with APOB or P4HB/PDI, partially inhibits triglyceride transfer activity, does not inhibit phospholipid transfer activity and apolipoprotein B secretion. 1 Publication1
Mutagenesisi435L → E: No loss on localization to the endoplasmic reticulum. Inhibits triglyceride transfer activity. 1 Publication1
Mutagenesisi435L → V: No loss on localization to the endoplasmic reticulum. Does not inhibit triglyceride transfer activity. 1 Publication1
Mutagenesisi528Y → F: Does not inhibit triglyceride transfer activity. 1 Publication1
Mutagenesisi528Y → K: Inhibits triglyceride transfer activity. 1 Publication1
Mutagenesisi540R → A: Strongly reduces triglyceride transfer activity. 1 Publication1
Mutagenesisi540R → K: Does not inhibit triglyceride transfer activity and apolipoprotein B secretion. 2 Publications1
Mutagenesisi878C → S: Inhibits triglyceride transfer activity. 1 Publication1

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNETi4547.
MalaCardsiMTTP.
MIMi200100. phenotype.
OpenTargetsiENSG00000138823.
Orphaneti14. Abetalipoproteinemia.
426. Familial hypobetalipoproteinemia.
PharmGKBiPA164742099.

Chemistry databases

ChEMBLiCHEMBL2569.
DrugBankiDB01094. Hesperetin.
DB08827. Lomitapide.

Polymorphism and mutation databases

BioMutaiMTTP.
DMDMi1709167.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 18Sequence analysisAdd BLAST18
ChainiPRO_000004159319 – 894Microsomal triglyceride transfer protein large subunitAdd BLAST876

Keywords - PTMi

Disulfide bond

Proteomic databases

EPDiP55157.
MaxQBiP55157.
PaxDbiP55157.
PeptideAtlasiP55157.
PRIDEiP55157.

PTM databases

iPTMnetiP55157.
PhosphoSitePlusiP55157.

Expressioni

Tissue specificityi

Liver and small intestine. Also found in ovary, testis and kidney.1 Publication

Inductioni

Positively regulated by cholesterol and negatively regulated by insulin.1 Publication

Gene expression databases

BgeeiENSG00000138823.
CleanExiHS_MTTP.
ExpressionAtlasiP55157. baseline and differential.
GenevisibleiP55157. HS.

Organism-specific databases

HPAiHPA054862.

Interactioni

Subunit structurei

Heterodimer; heterodimerizes with the protein disulfide isomerase (P4HB/PDI) (PubMed:23475612, PubMed:26224785, PubMed:25108285). Interacts with APOB (PubMed:26224785, PubMed:25108285, PubMed:27206948).4 Publications

GO - Molecular functioni

  • protein heterodimerization activity Source: UniProtKB

Protein-protein interaction databases

BioGridi110641. 4 interactors.
IntActiP55157. 1 interactor.
MINTiMINT-1537333.
STRINGi9606.ENSP00000265517.

Chemistry databases

BindingDBiP55157.

Structurei

3D structure databases

ProteinModelPortaliP55157.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini28 – 659VitellogeninPROSITE-ProRule annotationAdd BLAST632

Sequence similaritiesi

Contains 1 vitellogenin domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG4337. Eukaryota.
ENOG410YKCW. LUCA.
GeneTreeiENSGT00390000011412.
HOGENOMiHOG000113688.
HOVERGENiHBG006416.
InParanoidiP55157.
KOiK14463.
PhylomeDBiP55157.
TreeFamiTF328754.

Family and domain databases

Gene3Di1.25.10.20. 1 hit.
2.30.230.10. 1 hit.
InterProiIPR015819. Lipid_transp_b-sht_shell.
IPR001747. Lipid_transpt_N.
IPR015816. Vitellinogen_b-sht_N.
IPR011030. Vitellinogen_superhlx.
[Graphical view]
PfamiPF01347. Vitellogenin_N. 1 hit.
[Graphical view]
SMARTiSM00638. LPD_N. 1 hit.
[Graphical view]
SUPFAMiSSF48431. SSF48431. 1 hit.
SSF56968. SSF56968. 1 hit.
PROSITEiPS51211. VITELLOGENIN. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P55157-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MILLAVLFLC FISSYSASVK GHTTGLSLNN DRLYKLTYST EVLLDRGKGK
60 70 80 90 100
LQDSVGYRIS SNVDVALLWR NPDGDDDQLI QITMKDVNVE NVNQQRGEKS
110 120 130 140 150
IFKGKSPSKI MGKENLEALQ RPTLLHLIHG KVKEFYSYQN EAVAIENIKR
160 170 180 190 200
GLASLFQTQL SSGTTNEVDI SGNCKVTYQA HQDKVIKIKA LDSCKIARSG
210 220 230 240 250
FTTPNQVLGV SSKATSVTTY KIEDSFVIAV LAEETHNFGL NFLQTIKGKI
260 270 280 290 300
VSKQKLELKT TEAGPRLMSG KQAAAIIKAV DSKYTAIPIV GQVFQSHCKG
310 320 330 340 350
CPSLSELWRS TRKYLQPDNL SKAEAVRNFL AFIQHLRTAK KEEILQILKM
360 370 380 390 400
ENKEVLPQLV DAVTSAQTSD SLEAILDFLD FKSDSSIILQ ERFLYACGFA
410 420 430 440 450
SHPNEELLRA LISKFKGSIG SSDIRETVMI ITGTLVRKLC QNEGCKLKAV
460 470 480 490 500
VEAKKLILGG LEKAEKKEDT RMYLLALKNA LLPEGIPSLL KYAEAGEGPI
510 520 530 540 550
SHLATTALQR YDLPFITDEV KKTLNRIYHQ NRKVHEKTVR TAAAAIILNN
560 570 580 590 600
NPSYMDVKNI LLSIGELPQE MNKYMLAIVQ DILRFEMPAS KIVRRVLKEM
610 620 630 640 650
VAHNYDRFSR SGSSSAYTGY IERSPRSAST YSLDILYSGS GILRRSNLNI
660 670 680 690 700
FQYIGKAGLH GSQVVIEAQG LEALIAATPD EGEENLDSYA GMSAILFDVQ
710 720 730 740 750
LRPVTFFNGY SDLMSKMLSA SGDPISVVKG LILLIDHSQE LQLQSGLKAN
760 770 780 790 800
IEVQGGLAID ISGAMEFSLW YRESKTRVKN RVTVVITTDI TVDSSFVKAG
810 820 830 840 850
LETSTETEAG LEFISTVQFS QYPFLVCMQM DKDEAPFRQF EKKYERLSTG
860 870 880 890
RGYVSQKRKE SVLAGCEFPL HQENSEMCKV VFAPQPDSTS SGWF
Length:894
Mass (Da):99,351
Last modified:October 1, 1996 - v1
Checksum:iB20260C136BDAB9F
GO
Isoform 2 (identifier: P55157-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     134-151: EFYSYQNEAVAIENIKRG → GRLDSTTFSPTSYFSSLQ
     152-894: Missing.

Note: No experimental confirmation available.
Show »
Length:151
Mass (Da):16,865
Checksum:iF0A042FD95FA8F3A
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti585F → L in CAA42200 (PubMed:8361539).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_01401695Q → H.1 PublicationCorresponds to variant rs61733139dbSNPEnsembl.1
Natural variantiVAR_05296198E → D.Corresponds to variant rs2306986dbSNPEnsembl.1
Natural variantiVAR_014017128I → T.2 PublicationsCorresponds to variant rs3816873dbSNPEnsembl.1
Natural variantiVAR_052962166N → S.Corresponds to variant rs3792683dbSNPEnsembl.1
Natural variantiVAR_022658168V → I Rare polymorphism. 1 PublicationCorresponds to variant rs61750974dbSNPEnsembl.1
Natural variantiVAR_074553169D → V in ABL; no loss on localization to the endoplasmic reticulum; does not reduce interaction with APOB; inhibits interaction with P4HB/PDI; inhibits phospholipid or triglyceride transfer activity; inhibits apolipoprotein B secretion. 1 Publication1
Natural variantiVAR_014018244Q → E.1 PublicationCorresponds to variant rs17599091dbSNPEnsembl.1
Natural variantiVAR_074554264G → R in ABL; unknown pathological significance; does not reduce interaction with P4HB/PDI and APOB; does not reduce triglyceride transfer activity. 1 Publication1
Natural variantiVAR_010640297H → Q Polymorphism; does not inhibit apolipoprotein B secretion. 3 PublicationsCorresponds to variant rs2306985dbSNPEnsembl.1
Natural variantiVAR_014916354E → Q.Corresponds to variant rs12933dbSNPEnsembl.1
Natural variantiVAR_010641384D → A Polymorphism; no loss on localization to the endoplasmic reticulum; does not reduce interaction with P4HB/PDI; reduces phospholipid or triglyceride transfer activity; does not inhibit apolipoprotein B secretion. 2 PublicationsCorresponds to variant rs17029215dbSNPEnsembl.1
Natural variantiVAR_074555435L → H in ABL; no loss on localization to the endoplasmic reticulum; inhibits triglyceride transfer activity. 1 Publication1
Natural variantiVAR_074556528Y → H in ABL; does not reduce interaction with P4HB/PDI and APOB; inhibits triglyceride transfer activity. 1 Publication1
Natural variantiVAR_074557540R → C in ABL; does not reduce interaction with P4HB/PDI and APOB; inhibits triglyceride transfer activity. 1 PublicationCorresponds to variant rs372321643dbSNPEnsembl.1
Natural variantiVAR_010642540R → H in ABL; no loss on localization to the endoplasmic reticulum; reduces interaction with P4HB/PDI; inhibits phospholipid or triglyceride transfer activity; inhibits apolipoprotein B secretion. 4 PublicationsCorresponds to variant rs199422220dbSNPEnsembl.1
Natural variantiVAR_010643590S → I in ABL; no loss on localization to the endoplasmic reticulum; does not reduce interaction with P4HB/PDI; inhibits phospholipid or triglyceride transfer activity; inhibits apolipoprotein B secretion. 2 PublicationsCorresponds to variant rs199422222dbSNPEnsembl.1
Natural variantiVAR_074558649N → S in ABL; unknown pathological significance; does not reduce interaction with P4HB/PDI and APOB; reduces triglyceride transfer activity. 1 Publication1
Natural variantiVAR_010644746G → E in ABL; no loss on localization to the endoplasmic reticulum; does not reduce interaction with P4HB/PDI; inhibits phospholipid or triglyceride transfer activity; inhibits apolipoprotein B secretion. 2 PublicationsCorresponds to variant rs767833468dbSNPEnsembl.1
Natural variantiVAR_014019780N → Y in ABL; no loss on localization to the endoplasmic reticulum; does not reduce interaction with P4HB/PDI; inhibits phospholipid or triglyceride transfer activity; inhibits apolipoprotein B secretion. 2 PublicationsCorresponds to variant rs199422221dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_056325134 – 151EFYSY…NIKRG → GRLDSTTFSPTSYFSSLQ in isoform 2. 1 PublicationAdd BLAST18
Alternative sequenceiVSP_056326152 – 894Missing in isoform 2. 1 PublicationAdd BLAST743

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X75500 mRNA. Translation: CAA53217.1.
X59657 mRNA. Translation: CAA42200.1.
X83013
, X83014, X83015, X83016, X83017, X83018, X83019, X83020, X83021, X83022, X83023, X83024, X83025, X83026, X83027, X83028, X83029, X83030 Genomic DNA. Translation: CAA58142.1.
AK290793 mRNA. Translation: BAF83482.1.
AC083902 Genomic DNA. No translation available.
BC062696 mRNA. Translation: AAH62696.1.
BC125110 mRNA. Translation: AAI25111.1.
BC125111 mRNA. Translation: AAI25112.1.
CCDSiCCDS3651.1. [P55157-1]
PIRiI38047.
RefSeqiNP_000244.2. NM_000253.3. [P55157-1]
NP_001287714.1. NM_001300785.1.
UniGeneiHs.195799.

Genome annotation databases

EnsembliENST00000265517; ENSP00000265517; ENSG00000138823. [P55157-1]
ENST00000422897; ENSP00000407350; ENSG00000138823. [P55157-2]
ENST00000457717; ENSP00000400821; ENSG00000138823. [P55157-1]
GeneIDi4547.
KEGGihsa:4547.
UCSCiuc003hvb.4. human. [P55157-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X75500 mRNA. Translation: CAA53217.1.
X59657 mRNA. Translation: CAA42200.1.
X83013
, X83014, X83015, X83016, X83017, X83018, X83019, X83020, X83021, X83022, X83023, X83024, X83025, X83026, X83027, X83028, X83029, X83030 Genomic DNA. Translation: CAA58142.1.
AK290793 mRNA. Translation: BAF83482.1.
AC083902 Genomic DNA. No translation available.
BC062696 mRNA. Translation: AAH62696.1.
BC125110 mRNA. Translation: AAI25111.1.
BC125111 mRNA. Translation: AAI25112.1.
CCDSiCCDS3651.1. [P55157-1]
PIRiI38047.
RefSeqiNP_000244.2. NM_000253.3. [P55157-1]
NP_001287714.1. NM_001300785.1.
UniGeneiHs.195799.

3D structure databases

ProteinModelPortaliP55157.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110641. 4 interactors.
IntActiP55157. 1 interactor.
MINTiMINT-1537333.
STRINGi9606.ENSP00000265517.

Chemistry databases

BindingDBiP55157.
ChEMBLiCHEMBL2569.
DrugBankiDB01094. Hesperetin.
DB08827. Lomitapide.
SwissLipidsiSLP:000000411.

PTM databases

iPTMnetiP55157.
PhosphoSitePlusiP55157.

Polymorphism and mutation databases

BioMutaiMTTP.
DMDMi1709167.

Proteomic databases

EPDiP55157.
MaxQBiP55157.
PaxDbiP55157.
PeptideAtlasiP55157.
PRIDEiP55157.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000265517; ENSP00000265517; ENSG00000138823. [P55157-1]
ENST00000422897; ENSP00000407350; ENSG00000138823. [P55157-2]
ENST00000457717; ENSP00000400821; ENSG00000138823. [P55157-1]
GeneIDi4547.
KEGGihsa:4547.
UCSCiuc003hvb.4. human. [P55157-1]

Organism-specific databases

CTDi4547.
DisGeNETi4547.
GeneCardsiMTTP.
HGNCiHGNC:7467. MTTP.
HPAiHPA054862.
MalaCardsiMTTP.
MIMi157147. gene.
200100. phenotype.
neXtProtiNX_P55157.
OpenTargetsiENSG00000138823.
Orphaneti14. Abetalipoproteinemia.
426. Familial hypobetalipoproteinemia.
PharmGKBiPA164742099.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG4337. Eukaryota.
ENOG410YKCW. LUCA.
GeneTreeiENSGT00390000011412.
HOGENOMiHOG000113688.
HOVERGENiHBG006416.
InParanoidiP55157.
KOiK14463.
PhylomeDBiP55157.
TreeFamiTF328754.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000138823-MONOMER.
ReactomeiR-HSA-174800. Chylomicron-mediated lipid transport.
R-HSA-8866423. VLDL biosynthesis.

Miscellaneous databases

GeneWikiiMicrosomal_triglyceride_transfer_protein.
GenomeRNAii4547.
PROiP55157.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000138823.
CleanExiHS_MTTP.
ExpressionAtlasiP55157. baseline and differential.
GenevisibleiP55157. HS.

Family and domain databases

Gene3Di1.25.10.20. 1 hit.
2.30.230.10. 1 hit.
InterProiIPR015819. Lipid_transp_b-sht_shell.
IPR001747. Lipid_transpt_N.
IPR015816. Vitellinogen_b-sht_N.
IPR011030. Vitellinogen_superhlx.
[Graphical view]
PfamiPF01347. Vitellogenin_N. 1 hit.
[Graphical view]
SMARTiSM00638. LPD_N. 1 hit.
[Graphical view]
SUPFAMiSSF48431. SSF48431. 1 hit.
SSF56968. SSF56968. 1 hit.
PROSITEiPS51211. VITELLOGENIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiMTP_HUMAN
AccessioniPrimary (citable) accession number: P55157
Secondary accession number(s): A8K428, Q08AM4, Q6P5T3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: November 2, 2016
This is version 151 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 4
    Human chromosome 4: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.